WECC_PYRHO
ID WECC_PYRHO Reviewed; 418 AA.
AC O59284;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=UDP-N-acetyl-D-mannosamine dehydrogenase {ECO:0000303|PubMed:25305481};
DE Short=UDP-D-ManNAcDH {ECO:0000303|PubMed:25305481};
DE EC=1.1.1.336 {ECO:0000250|UniProtKB:Q6LZC3};
DE AltName: Full=UDP-ManNAc 6-dehydrogenase {ECO:0000305};
GN OrderedLocusNames=PH1618 {ECO:0000312|EMBL:BAA30730.1};
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP CRYSTALLIZATION, AND SUBUNIT.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=17565184; DOI=10.1107/s1744309107016685;
RA Lokanath N.K., Pampa K.J., Kamiya T., Kunishima N.;
RT "Purification, crystallization and preliminary X-ray diffraction studies of
RT a putative UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus
RT horikoshii OT3.";
RL Acta Crystallogr. F 63:412-414(2007).
RN [3] {ECO:0007744|PDB:4R16}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH THE PRODUCT
RP UDP-D-MANNACA, FUNCTION, DOMAIN, AND ACTIVE SITE.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=25305481; DOI=10.1016/j.bbrc.2014.10.010;
RA Pampa K.J., Lokanath N.K., Girish T.U., Kunishima N., Rai V.R.;
RT "Crystal structure of product-bound complex of UDP-N-acetyl-d-mannosamine
RT dehydrogenase from Pyrococcus horikoshii OT3.";
RL Biochem. Biophys. Res. Commun. 453:662-667(2014).
CC -!- FUNCTION: Catalyzes the four-electron oxidation of UDP-N-acetyl-D-
CC mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N-
CC acetylmannosaminuronic acid (UDP-ManNAcA).
CC {ECO:0000250|UniProtKB:Q6LZC3, ECO:0000305|PubMed:25305481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 2 NAD(+) + UDP-N-acetyl-alpha-D-mannosamine = 3 H(+) + 2
CC NADH + UDP-N-acetyl-alpha-D-mannosaminouronate; Xref=Rhea:RHEA:25780,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:68623, ChEBI:CHEBI:70731;
CC EC=1.1.1.336; Evidence={ECO:0000250|UniProtKB:Q6LZC3};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17565184}.
CC -!- DOMAIN: The protomer folds into three distinct domains: an N-terminal
CC nucleotide binding domain, a central helical domain involved in
CC dimerization and a C-terminal substrate binding domain.
CC {ECO:0000269|PubMed:25305481}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; BA000001; BAA30730.1; -; Genomic_DNA.
DR PIR; B71041; B71041.
DR RefSeq; WP_010885691.1; NC_000961.1.
DR PDB; 4R16; X-ray; 1.55 A; A/B=1-418.
DR PDBsum; 4R16; -.
DR AlphaFoldDB; O59284; -.
DR SMR; O59284; -.
DR STRING; 70601.3258047; -.
DR EnsemblBacteria; BAA30730; BAA30730; BAA30730.
DR GeneID; 1442470; -.
DR KEGG; pho:PH1618; -.
DR eggNOG; arCOG00252; Archaea.
DR OMA; IELANTH; -.
DR OrthoDB; 41144at2157; -.
DR BRENDA; 1.1.1.336; 5244.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0089714; F:UDP-N-acetyl-D-mannosamine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017476; UDP-Glc/GDP-Man.
DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR InterPro; IPR028359; UDP_ManNAc/GlcNAc_DH.
DR Pfam; PF00984; UDPG_MGDP_dh; 1.
DR Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR PIRSF; PIRSF500136; UDP_ManNAc_DH; 1.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52413; SSF52413; 1.
DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase.
FT CHAIN 1..418
FT /note="UDP-N-acetyl-D-mannosamine dehydrogenase"
FT /id="PRO_0000443382"
FT REGION 152..153
FT /note="Substrate"
FT /evidence="ECO:0000269|PubMed:25305481,
FT ECO:0007744|PDB:4R16"
FT REGION 208..211
FT /note="Substrate"
FT /evidence="ECO:0000269|PubMed:25305481,
FT ECO:0007744|PDB:4R16"
FT REGION 242..244
FT /note="Substrate; shared with dimeric partner"
FT /evidence="ECO:0000269|PubMed:25305481,
FT ECO:0007744|PDB:4R16"
FT REGION 318..319
FT /note="Substrate"
FT /evidence="ECO:0000269|PubMed:25305481,
FT ECO:0007744|PDB:4R16"
FT ACT_SITE 204
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:25305481"
FT ACT_SITE 258
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:25305481"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25305481,
FT ECO:0007744|PDB:4R16"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4R16"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25305481,
FT ECO:0007744|PDB:4R16"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25305481,
FT ECO:0007744|PDB:4R16"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:4R16"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:4R16"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:4R16"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 197..228
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:4R16"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 287..301
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:4R16"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 375..379
FT /evidence="ECO:0007829|PDB:4R16"
FT HELIX 382..387
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 393..399
FT /evidence="ECO:0007829|PDB:4R16"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:4R16"
SQ SEQUENCE 418 AA; 46134 MW; CA7C5903610D2382 CRC64;
MRIAVLGLGY IGLPTAIMFA SSGYDVVGYD IRSEVIKKIN SGVAHIIEPE IDRRLKEVLS
LGKLKVTDRV EDLKGSNVFI ICVQTPLSGD DPDLSYLERA IRTVAEVMDR GALVIIESTI
PPGTTEKMAR LLENLTGLRE GVDFYVAHAP ERVMPGRIFK ELVYNSRIIG GVSEKAANLA
EKLYRSFVKG RIFLTNATTA EMVKLMENTF RDVNIALANE FALLAHQYGV NVYEAIELAN
THPRVKIHTP GIGVGGHCLP KDPYLLLSNA KEDFGLIRIA RRINERMPAF AAGLLFEALE
KANIKPSEAI IAVLGLAYKG GTDDTRNSPA LKFVEIIRNS VKEVRTYDPY VRGTHDSLEK
VVEGADAIVI ATDHPEFKSV NWESIGKSMR HKIIIDGRNI IKEPPVGFIF RGIGRGDV
